Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement

The ubiquitous protein chaperone hsp90 has been shown to regulate more than 100 proteins involved in cellular signalling. These proteins are called 'client proteins' for hsp90, and a multiprotein hsp90/hsp70-based chaperone machinery forms client protein.hsp90 heterocomplexes in the cytopl...

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Autores: Pratt, William B., Galigniana, Mario Daniel, Harrell, Jennifer M., de Franco, Donald B.
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2004
País:Argentina
Recursos:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/29102
Acesso em linha:http://hdl.handle.net/11336/29102
Access Level:acceso abierto
Palavra-chave:https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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spelling Role of hsp90 and the hsp90-binding immunophilins in signalling protein movementPratt, William B.Galigniana, Mario DanielHarrell, Jennifer M.de Franco, Donald B.https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The ubiquitous protein chaperone hsp90 has been shown to regulate more than 100 proteins involved in cellular signalling. These proteins are called 'client proteins' for hsp90, and a multiprotein hsp90/hsp70-based chaperone machinery forms client protein.hsp90 heterocomplexes in the cytoplasm and the nucleus. In the case of signalling proteins that act as transcription factors, the client protein.hsp90 complexes also contain one of several TPR domain immunophilins or immunophilin homologs that bind to a TPR domain binding site on hsp90. Using several intracellular receptors and the tumor suppressor p53 as examples, we review evidence that dynamic assembly of heterocomplexes with hsp90 is required for rapid movement through the cytoplasm to the nucleus along microtubular tracks. The role of the immunophilin in this system is to connect the client protein.hsp90 complex to cytoplasmic dynein, the motor protein for retrograde movement toward the nucleus. Upon arrival at the nuclear pores, the receptor.hsp90.immunophilin complexes are transferred to the nuclear interior by importin-dependent facilitated diffusion. The unliganded receptors then distribute within the nucleus to diffuse patches from which they proceed in a ligand-dependent manner to discrete nuclear foci where chromatin binding occurs. We review evidence that dynamic assembly of heterocomplexes with hsp90 is required for movement to these foci and for the dynamic exchange of transcription factors between chromatin and the nucleoplasm.Fil: Pratt, William B.. University of Michigan; Estados UnidosFil: Galigniana, Mario Daniel. University of Michigan; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Harrell, Jennifer M.. University of Michigan; Estados UnidosFil: de Franco, Donald B.. University of Pittsburgh; Estados UnidosElsevier Inc2004info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/29102Pratt, William B.; Galigniana, Mario Daniel; Harrell, Jennifer M.; de Franco, Donald B.; Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement; Elsevier Inc; Cellular Signalling; 16; 8; -1-2004; 857-8720898-65681873-3913CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0898656804000257?via%3Dihubinfo:eu-repo/semantics/altIdentifier/url/10.1016/j.cellsig.2004.02.004info:eu-repo/semantics/altIdentifier/pmid/15157665info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:45:18Zoai:ri.conicet.gov.ar:11336/29102instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982024-05-08 13:45:18.914CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
title Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
spellingShingle Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
Pratt, William B.
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
title_short Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
title_full Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
title_fullStr Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
title_full_unstemmed Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
title_sort Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
dc.creator.none.fl_str_mv Pratt, William B.
Galigniana, Mario Daniel
Harrell, Jennifer M.
de Franco, Donald B.
author Pratt, William B.
author_facet Pratt, William B.
Galigniana, Mario Daniel
Harrell, Jennifer M.
de Franco, Donald B.
author_role author
author2 Galigniana, Mario Daniel
Harrell, Jennifer M.
de Franco, Donald B.
author2_role author
author
author
dc.subject.none.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
description The ubiquitous protein chaperone hsp90 has been shown to regulate more than 100 proteins involved in cellular signalling. These proteins are called 'client proteins' for hsp90, and a multiprotein hsp90/hsp70-based chaperone machinery forms client protein.hsp90 heterocomplexes in the cytoplasm and the nucleus. In the case of signalling proteins that act as transcription factors, the client protein.hsp90 complexes also contain one of several TPR domain immunophilins or immunophilin homologs that bind to a TPR domain binding site on hsp90. Using several intracellular receptors and the tumor suppressor p53 as examples, we review evidence that dynamic assembly of heterocomplexes with hsp90 is required for rapid movement through the cytoplasm to the nucleus along microtubular tracks. The role of the immunophilin in this system is to connect the client protein.hsp90 complex to cytoplasmic dynein, the motor protein for retrograde movement toward the nucleus. Upon arrival at the nuclear pores, the receptor.hsp90.immunophilin complexes are transferred to the nuclear interior by importin-dependent facilitated diffusion. The unliganded receptors then distribute within the nucleus to diffuse patches from which they proceed in a ligand-dependent manner to discrete nuclear foci where chromatin binding occurs. We review evidence that dynamic assembly of heterocomplexes with hsp90 is required for movement to these foci and for the dynamic exchange of transcription factors between chromatin and the nucleoplasm.
publishDate 2004
dc.date.none.fl_str_mv 2004
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/29102
Pratt, William B.; Galigniana, Mario Daniel; Harrell, Jennifer M.; de Franco, Donald B.; Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement; Elsevier Inc; Cellular Signalling; 16; 8; -1-2004; 857-872
0898-6568
1873-3913
CONICET Digital
CONICET
url http://hdl.handle.net/11336/29102
identifier_str_mv Pratt, William B.; Galigniana, Mario Daniel; Harrell, Jennifer M.; de Franco, Donald B.; Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement; Elsevier Inc; Cellular Signalling; 16; 8; -1-2004; 857-872
0898-6568
1873-3913
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0898656804000257?via%3Dihub
info:eu-repo/semantics/altIdentifier/url/10.1016/j.cellsig.2004.02.004
info:eu-repo/semantics/altIdentifier/pmid/15157665
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Inc
publisher.none.fl_str_mv Elsevier Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 15,811543

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